Structure of PDB 5e9z Chain D Binding Site BS01

Receptor Information
>5e9z Chain D (length=444) Species: 1404 (Priestia megaterium) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGLVTRYL
SSQRLIKEACDGSRFDKNLSQALKFVRDIAGDGLVTSWTHEKNWKKAHNI
LLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPGDMTRLTLDT
IGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKQQACDENKRQFQEDI
KVMNDLVDKIIADRKAQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFL
IAGHVTTSGLLSFALYFLVKNPYVLQKAAEEAARVLVDPVPSYKQVKQLK
YVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHR
DKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATL
VLSMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLG
Ligand information
Ligand IDPP9
InChIInChI=1S/C34H34N4O4/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25/h7-8,13-16,36-37H,1-2,9-12H2,3-6H3,(H,39,40)(H,41,42)/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-
InChIKeyFEDYMSUPMFCVOD-UJJXFSCMSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1c2[nH]c(cc3nc(cc4[nH]c(cc5nc(c2)c(C)c5C=C)c(C)c4C=C)c(C)c3CCC(O)=O)c1CCC(O)=O
OpenEye OEToolkits 1.5.0Cc1c2cc3nc(cc4c(c(c([nH]4)cc5nc(cc(c1CCC(=O)O)[nH]2)C(=C5C)CCC(=O)O)C=C)C)C(=C3C)C=C
ACDLabs 10.04O=C(O)CCc5c2nc(cc4nc(cc1c(c(\C=C)c(n1)cc3nc(c2)C(=C3C)CCC(=O)O)C)C(\C=C)=C4C)c5C
OpenEye OEToolkits 1.5.0Cc1c2\cc\3/nc(\cc/4\c(c(/c(/[nH]4)c/c5n/c(c\c(c1CCC(=O)O)[nH]2)/C(=C5C)CCC(=O)O)C=C)C)C(=C3C)C=C
FormulaC34 H34 N4 O4
NamePROTOPORPHYRIN IX
ChEMBLCHEMBL1618319
DrugBank
ZINC
PDB chain5e9z Chain D Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5e9z Insights into regioselective metabolism of mefenamic acid by cytochrome P450 BM3 mutants through crystallography, docking, molecular dynamics, and free energy calculations.
Resolution2.23 Å
Binding residue
(original residue number in PDB)		K69 L86 V87 W96 F107 F261 A264 G265 T268 A328 F331 P392 F393 R398 C400 I401 G402 A406
Binding residue
(residue number reindexed from 1)		K67 L84 V85 W94 F105 F249 A252 G253 T256 A316 F319 P380 F381 R386 C388 I389 G390 A394
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) T268 F393 C400
Catalytic site (residue number reindexed from 1) T256 F381 C388
Enzyme Commision number 1.14.14.1: unspecific monooxygenase.
1.6.2.4: NADPH--hemoprotein reductase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding

View graph for
Molecular Function
External links
PDB RCSB:5e9z, PDBe:5e9z, PDBj:5e9z
PDBsum5e9z
PubMed26757175
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

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